Drug intelligence / Profile preview

gp96-Ig (NightHawk Biosciences, Inc.)

Development stage
Unknown
Lead developer
University of Miami
Modality
Fc-Fusion Proteins → Carrier/Scaffold Proteins → Recombinant Proteins and Enzymes
Administration
Intradermal, Subcutaneous, Intraperitoneal
01

Overview

gp96-Ig (also referred to as gp96IgG or gp96-IgG) is an engineered recombinant fusion protein consisting of the endoplasmic reticulum chaperone heat shock protein gp96 (endoplasmin/grp94) fused to the Fc portion (hinge, CH2, and CH3 domains) of immunoglobulin G1 (IgG1). Originally developed at the University of Miami Miller School of Medicine by Dr. Eckhard Podack and licensed to Heat Biologics, gp96-Ig serves as a versatile vaccine platform. By replacing the C-terminal KDEL endoplasmic retention signal of gp96 with the IgG Fc tag, the fusion protein is continuously secreted from transfected cells. Secreted gp96-Ig acts as a potent biological adjuvant and antigen chaperone, binding to cell-associated peptides and delivering them to antigen-presenting cells (APCs) via CD91-receptor-mediated endocytosis. This facilitates highly efficient MHC class I cross-presentation and activates robust, antigen-specific CD8+ cytotoxic T lymphocyte (CTL) and NK cell responses, as well as mucosal and systemic immunity, without requiring CD4+ T cell help.

Other names
endoplasmin-IgG fusion proteinglycoprotein 96-immunoglobulin Gglycoprotein96-immunoglobulin Gglycoprotein-96-immunoglobulin Ggp96-vaccinegp-96-vaccinegp 96-vaccine
02

Targets

TLR2 (Toll-like Receptor 2)LRP1 (Prolow-density lipoprotein receptor-related protein 1)TLR4 (Toll-like receptor 4)

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